NMR paper 1H, 15N and 13C NMR resonance assignments of staphostatin A, a specific Staphylococcu

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[NMR paper] 1H, 15N and 13C NMR resonance assignments of staphostatin A, a specific Staphylococcu

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NMR processing:

MDD

NMR assignment:

Backbone:

Side-chains:

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Rosetta-NMR (Robetta)

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Promega- Proline

Secondary structure from chemical shifts:

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TALOS

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d2D

PECAN

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Proshift

PPM

CheShift-2- Cα

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Shifty

Camcoil

Poulsen_rc_CS

Disordered proteins:

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11-24-2010, 09:25 PM

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1H, 15N and 13C NMR resonance assignments of staphostatin A, a specific Staphylococcu

1H, 15N and 13C NMR resonance assignments of staphostatin A, a specific Staphylococcus aureus cysteine proteinase inhibitor.

Related Articles 1H, 15N and 13C NMR resonance assignments of staphostatin A, a specific Staphylococcus aureus cysteine proteinase inhibitor.

J Biomol NMR. 2004 Mar;28(3):295-6

Authors: Dubin G, Popowicz G, Krajewski M, Potempa J, Dubin A, Holak TA

The increasing antibiotic resistance of an important human pathogen Staphylococcus aureus calls for the development of new therapeutic strategies. Staphylococcal cysteine proteases have been suggested as targets for such therapies. The recent discovery of staphostatins, specific protein inhibitors of these enzymes, gives prospects for the design and production of synthetic, low molecular weight analogs which might become drugs. We have decided to structurally characterize staphostatin A, a representative inhibitor of staphylococcal cysteine proteases, and to assess its binding mode to the target protease with the view of clarifying the specificity determinants. Here we report the (1)H, (15)N and (13)C NMR resonance assignments of staphostatin A.

PMID: 14752262 [PubMed - indexed for MEDLINE]

Source: PubMed

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